ID A0A0S9E022_9MICO Unreviewed; 698 AA.
AC A0A0S9E022;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN ORFNames=ASF06_02195 {ECO:0000313|EMBL:KQO11484.1};
OS Agreia sp. Leaf244.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO11484.1, ECO:0000313|Proteomes:UP000051484};
RN [1] {ECO:0000313|EMBL:KQO11484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11484.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO11484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO11484.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412,
CC ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQO11484.1}.
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DR EMBL; LMLX01000001; KQO11484.1; -; Genomic_DNA.
DR RefSeq; WP_055942760.1; NZ_LMLX01000001.1.
DR AlphaFoldDB; A0A0S9E022; -.
DR STRING; 1736305.ASF06_02195; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000051484; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013739; Beta_galactosidase_C.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT DOMAIN 18..394
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 408..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 652..697
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 698 AA; 77513 MW; 31E1977D3D6C7169 CRC64;
MQRRFPALTD RILFGAAYYA EYQRSGTLDR DLDLMVEAGF TVIRVGESVW STWEPRDGEF
DLEWLLPVLD GAHARGISVI LGTPTYAVPP WLQRIHPEIA AENADGSTVG WGQRQEMDYS
HPTFRWYAER IIRAVVGRYA EHPAVIGYQV DNEPGQQLAH NHHVMQGFLE WLRAKYGTLE
NLNEQWGLVY WSHRLSEWAD LWTPKGNLQP QYALEWRRYH SALVTDFIGW EADIVREYAN
DGQFVTTCIS YNRPPVSDDE LVERLDITAG NPYYRMQDGL SNVVETRADA PWWTSGPWAL
FGQADRMYST SQDRFLVTET NAQSIGGHWQ NQPPYPGQIV QAGLALVSRG ARMIEYWHWH
TLHFGVETYW GGVLPHSQRP GRIYREVAEL GSILGTLGSE LEGYTPSADA AIIWSTDTRW
SFQSYPPLAK PDGDRDPESY QRIYDSFYRG AHDAGLQLRV LHDRQFAALD PAELARDIPI
LFAPAVYVAD DALLDQLRAY AEAGGHLVLG PRTGYGDELA RARRGVAPDR LAEAAGAWYE
EYSNLDAPVS VVSTGQLELA PSASATAWAD GVIADGAEVL ATYDHHFLGR FAAVTSTPFG
AGRITYVGTV PDAGLSSSVA RWVKGDTVKT GWPVPAAVSV VSGSSDAHDA IWFVHNWSPD
AVTVTAPASL TDLVDGAAVA HGSDILLAPW SVRVLSED
//
